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Inside Cover: Primary Steps of pH-Dependent Insulin Aggregation Kinetics are Governed by Conformational Flexibility (ChemBioChem 11/2009)
The inside cover picture shows, on the left, the structure of peptide hormone insulin; titrable groups between pH 1 to 7 are highlighted. On the right, structural ensembles from atomistic simulations show that pH-induced protonation changes of insulin critically affect its conformational flexibility. From top to bottom the number of protonated sites was increased to match displayed pH values. For more information, see the article by H. Grubmüller et al. on p. 1816 ff.